Peptidimer d seemed to have probably the most powerful inhibition on K562 cells at 6 h, while Gleevec at 24 h. Within the last few part, we showed that peptidimer h activated caspase three and the apoptosis in K562 cells. To be able to further date=june 2011 the effect of caspase inhibitor on the cells treated with peptidimer c, FCM assay was fluorescent peptides performed to evaluate the effect ofn K562 cell cycle of K562 successively treated with 20 mM of Z VAD fmk for 2 h and then with increasing doses of peptidimer c for 6 h and 24 h. These results suggest that caspase 3 inhibitor affected the distribution of K562 cell cycle phases addressed with peptidimer h. These results also help that apoptosis is mediated by peptidimer h connected with caspase 3 activation. Since cell cycle progression requires the co ordinated interaction and activation of cyclins and cyclin dependent kinases, the expression levels of cyclin A, Cdk2, phospho Cdk2, cyclin B, Cdk1, and phospho Cdk1 was analyzed by western blot analysis after K562 cells treatment for 6 h with potent FAAH inhibitor different amounts of both peptidimer h or penetratin vector alone as a control. Cyclin A expression was demonstrably decreased after peptidimer h therapy. While total Cdk2 level was constant throughout treatment with low concentrations of peptidimer c, it slightly reduced for a focus of 27 mM. Phospho Cdk2 plainly reduced after peptidimer c therapy, first and foremost for 27 mM of peptidimer c. No effectation of peptidimer d treatment was found neither in Cdk1 nor in its phosphorylated form. No effect was observed in cyclin B and cyclin D levels in the same circumstances. In most studies, actin degree was verified to be constant. No significant difference was observed in the appearance of any of the studied proteins, demonstrating the specificity of peptidimer d, when cells were treated by Urogenital pelvic malignancy penetratin vector. D showed the expression levels of cell cycle related molecules in K562 cells treated with different levels of imatinib for 24 h. It was found by western blot assay that the degree of cyclin D, cyclin B got obviously decline in a dose dependent setting. There appeared no modifications for the cyclin A, Cdk1, and Cdk2. Nevertheless the significant decrease of p Cdk2 and p Cdk1 was observed. These results support different impact on K562 cell cycle of peptidimer d and imatinib. Inspite of the efficacy of imatinib, some people in higher level phases of CML and more in chronic phase maintain enzymatic activity, often as a result of Bcr Abl tyrosine kinase domain mutations that impair imatinib binding and create resistance. It’s therefore crucial that you offer alternative therapeutics. New tyrosine kinase inhibitors that inhibit natural product libraries Bcr Abl more potently than imatinib have already been created and maintain activity against a range of imatinibresistant Bcr Abl mutants.